PMID:12077450
| Citation |
Urbina, HD, Cupp-Vickery, JR and Vickery, LE (2002) Preliminary crystallographic analysis of the cysteine desulfurase IscS from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:1224-5 |
|---|---|
| Abstract |
IscS is a widely distributed cysteine desulfurase that catalyzes the pyridoxal phosphate dependent beta-elimination of sulfur from L-cysteine and plays a central role in the delivery of sulfur to a variety of metabolic pathways. Crystals of Escherichia coli IscS have been obtained by the hanging-drop vapor-diffusion method using polyethylene glycol (PEG) as a precipitant. Initial seed crystals were obtained using PEG 6000 and sodium acetate, and diffraction-quality crystals were grown using a mixture of PEG 2000 and PEG 10 000 in the presence of sodium citrate. A complete native X-ray diffraction data set was collected from a single crystal at 103 K to a resolution of 2.1 A. The crystals belong to space group P2(1)2(1)2(1) and have unit-cell parameters a = 73.7086, b = 101.9741, c = 108.617 A (alpha = beta = gamma = 90 degrees ). Analysis of the Matthews equation and self-rotation function suggest two molecules per asymmetric unit, consistent with the presence of a single dimeric molecule. |
| Links | |
| Keywords |
Carbon-Sulfur Lyases/chemistry; Catalytic Domain; Crystallography, X-Ray/methods; Dimerization; Escherichia coli/enzymology; Polyethylene Glycols/chemistry |
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